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This study developed a new human iPSC model for tauopathies, identifying pinin (PNN) and other RNA binding proteins as key regulators of tau aggregation and neuronal toxicity in Alzheimer's disease and PSP.

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Genetics

Background:

  • Tauopathies, including Alzheimer's disease (AD) and progressive supranuclear palsy (PSP), involve tau protein aggregation and neuronal loss.
  • Existing human induced pluripotent stem cell (iPSC)-derived neuron models struggle to replicate higher-order tau aggregates, limiting research into aggregation mechanisms and toxicity.

Purpose of the Study:

  • To develop a novel iPSC-based model system for studying tau aggregation and toxicity in tauopathies.
  • To identify novel genetic regulators involved in tau aggregation and associated neuronal dysfunction.

Main Methods:

  • Established a human iPSC line (WTC11) engineered to express tau protein (FL-tau).
  • Induced tau aggregation in iPSCs and differentiated neurons by introducing tau aggregates from PSP patient brain lysate.
  • Utilized bulk proteomics and CRISPR interference (CRISPRi) screening to identify genes modulating tau aggregation.

Main Results:

  • The novel model successfully propagated tau aggregates in iPSCs and differentiated neurons.
  • Proteomics revealed enrichment of splicing-related RNA binding proteins (RBPs), notably pinin (PNN), in aggregated tau neurons.
  • Pinin (PNN) mis-localized to cytoplasmic tau inclusions in iNeurons and human AD/PSP brain tissue, with reduced nuclear staining.
  • CRISPRi screening identified novel RBPs, including those involved in stress granules and RNA metabolism, as regulators of tau aggregation.

Conclusions:

  • Identified pinin (PNN) and stress granule-related proteins as novel regulators of tau aggregation and toxicity.
  • Demonstrated the utility of the novel iPSC model for tauopathy research.
  • Highlighted the potential role of altered PNN localization in tauopathy pathogenesis.